FGF Basic (Fibroblast Growth Factor) ELISA

pFGF Basic (Fibroblast Growth br /
Factor) ELISAbr /
img alt=For Research Use Only align=absMiddle src=http://www.alpco.com/img/ruo.gif / For Research Use Only/p
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div class=prod_specbFormat:/b/div
div class=prod_spec_infoELISA / EIA/div
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div class=prod_specSample Type:/div
div class=prod_spec_infoserum, plasma, cell culture/div
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div class=prod_specbSample Size:/b/div
div class=prod_spec_info50 micro;l/div
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div class=prod_specbSize:/b/div
div class=prod_spec_info96 wells/div
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div class=prod_specbRange:/b/div
div class=prod_spec_info15.6 - 1000 pg/ml/div
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div class=prod_specbSensitivity:/b/div
div class=prod_spec_info7 pg/ml/div
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div class=prod_specbIncubation Time:/b/div
div class=prod_spec_info4 Hour/div
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pbSummary:/b/p
The family of Fibroblast Growth Factors (FGFs) includes at least 13 known polypeptides that share up to 55% amino acid sequence homology and are highly conserved among species. FGFs are involved in many physiological and pathological processes including embryonic development, neuronal outgrowth, angiogenesis and malignant transformation. Basic Fibroblast Growth Factor (FGF-b or FGF-2) exist as five isoforms with distinct intracellular localizations and functions. The 18 kDa isoform is predominantly cytosolic and acts through cell surface receptors, whereas the 22, 22.5, 24 and 34 kDa isoforms are nuclear and may signal independently of transmembrane receptor pathways. br /
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The five FGF-b isoforms differ only in their N-terminal region, as a result of being synthesized by alternative translation initiation. FGF-b is essential for the development and maintenance of vascular integrity during embryogenesis and is also a major angiogenic factor involved in wound healing, cardiovascular disease and tumor neovascularization. Fibroblast growth factors cause a cellular response through their interactions with high-affinity transmembrane receptors. Four FGF receptors have been identified to date. The structure of these receptors includes an extracellular domain, a transmembrane domain, and a cytoplasmic tyrosine kinase domain. The extracellular domain, which consists of two or three immunoglobulin-like loops, interacts with the FGF ligand. There is approximately 80% amino acid homology within the ligand-binding and tyrosine kinase domains of the four receptors. After FGF binding, the receptors dimerize leading to autophosphorylation of the cytoplasmic domains of the receptors./div
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